ID   ECTC_TERTT              Reviewed;         132 AA.
AC   C5BQN7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=L-ectoine synthase {ECO:0000255|HAMAP-Rule:MF_01255};
DE            EC=4.2.1.108 {ECO:0000255|HAMAP-Rule:MF_01255};
DE   AltName: Full=N-acetyldiaminobutyrate dehydratase {ECO:0000255|HAMAP-Rule:MF_01255};
GN   Name=ectC {ECO:0000255|HAMAP-Rule:MF_01255}; OrderedLocusNames=TERTU_3380;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
CC   -!- FUNCTION: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-
CC       diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-
CC       pyrimidine carboxylic acid), which is an excellent osmoprotectant.
CC       {ECO:0000255|HAMAP-Rule:MF_01255}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine;
CC         Xref=Rhea:RHEA:17281, ChEBI:CHEBI:15377, ChEBI:CHEBI:58515,
CC         ChEBI:CHEBI:58929; EC=4.2.1.108; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01255};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 3/3. {ECO:0000255|HAMAP-
CC       Rule:MF_01255}.
CC   -!- SIMILARITY: Belongs to the ectoine synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01255}.
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DR   EMBL; CP001614; ACR13313.1; -; Genomic_DNA.
DR   RefSeq; WP_015819426.1; NC_012997.1.
DR   AlphaFoldDB; C5BQN7; -.
DR   SMR; C5BQN7; -.
DR   STRING; 377629.TERTU_3380; -.
DR   EnsemblBacteria; ACR13313; ACR13313; TERTU_3380.
DR   KEGG; ttu:TERTU_3380; -.
DR   eggNOG; COG1917; Bacteria.
DR   HOGENOM; CLU_154525_0_0_6; -.
DR   OMA; CVFNPPI; -.
DR   OrthoDB; 1928636at2; -.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000009080; Chromosome.
DR   GO; GO:0033990; F:ectoine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06978; cupin_EctC; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_01255; Ectoine_synth; 1.
DR   InterPro; IPR010462; Ectoine_synth.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR39289; PTHR39289; 1.
DR   Pfam; PF06339; Ectoine_synth; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..132
FT                   /note="L-ectoine synthase"
FT                   /id="PRO_1000214119"
SQ   SEQUENCE   132 AA;  15210 MW;  E25C94AEDFFEE1C9 CRC64;
     MIVRNLTEAR DSNRRIVSPD GNWESTRMLL KDDKMGFSFH ITTIYKGADF RMHYQNHLES
     VYCVRGRGEV ETLADGKKYP IEPGTLYILD KHDEHMLRAF EEMEMACVFN PPLNGTEVHN
     AEGAYELNAE AL